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A0L3M0

- BIOB_MAGSM

UniProt

A0L3M0 - BIOB_MAGSM

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Protein

Biotin synthase

Gene

bioB

Organism
Magnetococcus sp. (strain MC-1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.UniRule annotation

Catalytic activityi

Dethiobiotin + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine = biotin + (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • [4Fe-4S] clusterUniRule annotationNote: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.UniRule annotation
  • [2Fe-2S] clusterUniRule annotationNote: Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi59 – 591Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi63 – 631Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi66 – 661Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi103 – 1031Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi135 – 1351Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi195 – 1951Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi265 – 2651Iron-sulfur 2 (2Fe-2S)UniRule annotation

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
  2. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  3. biotin synthase activity Source: UniProtKB-HAMAP
  4. iron ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. biotin biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Biotin biosynthesis

Keywords - Ligandi

2Fe-2S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciMSP156889:GH36-34-MONOMER.
UniPathwayiUPA00078; UER00162.

Names & Taxonomyi

Protein namesi
Recommended name:
Biotin synthaseUniRule annotation (EC:2.8.1.6UniRule annotation)
Gene namesi
Name:bioBUniRule annotation
Ordered Locus Names:Mmc1_0034
OrganismiMagnetococcus sp. (strain MC-1)
Taxonomic identifieri156889 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaMagnetococcalesMagnetococcaceaeMagnetococcus
ProteomesiUP000002586: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 321321Biotin synthasePRO_0000381452Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi156889.Mmc1_0034.

Structurei

3D structure databases

ProteinModelPortaliA0L3M0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the radical SAM superfamily. Biotin synthase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239958.
KOiK01012.
OMAiTCENTLR.
OrthoDBiEOG622PMP.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01694. BioB.
InterProiIPR013785. Aldolase_TIM.
IPR010722. BATS_dom.
IPR002684. Biotin_synth/BioAB.
IPR024177. Biotin_synthase.
IPR006638. Elp3/MiaB/NifB.
IPR007197. rSAM.
[Graphical view]
PfamiPF06968. BATS. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF001619. Biotin_synth. 1 hit.
SMARTiSM00876. BATS. 1 hit.
SM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00433. bioB. 1 hit.

Sequencei

Sequence statusi: Complete.

A0L3M0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAEAALAGQL PDAQSGLRLL TDPGIELLPL LQAAFRVRFH HFGRGVRIHI
60 70 80 90 100
LNNVQNGYCS EDCNYCAQAK NSKAPIEKYS IKSDEEILEG ARKAYESGAY
110 120 130 140 150
RYCMVSSGRS PHAERIDHMS KLIREIKSRW PVEVCLSAGF LDANKARELK
160 170 180 190 200
EAGLDRYNHN LNTADGYYGS ICTTHSYGDR LNTLQEARRA GLEVCSGIII
210 220 230 240 250
GMGEKPEEIV EVATTLRSLQ ARSIPVNFYV HVEGAQLGAV DQLTPAYALR
260 270 280 290 300
ALALFRFFNP DAEVRAAGGR ESNLRGMESM ALYPANSLFA EGYLNTTGHM
310 320
AEKTVKMVED AGFFVEKIEE E
Length:321
Mass (Da):35,530
Last modified:December 12, 2006 - v1
Checksum:iC6EC58487D65BB4C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000471 Genomic DNA. Translation: ABK42563.1.
RefSeqiYP_863969.1. NC_008576.1.

Genome annotation databases

EnsemblBacteriaiABK42563; ABK42563; Mmc1_0034.
GeneIDi4480720.
KEGGimgm:Mmc1_0034.
PATRICi22426524. VBIMagSp23654_0034.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000471 Genomic DNA. Translation: ABK42563.1 .
RefSeqi YP_863969.1. NC_008576.1.

3D structure databases

ProteinModelPortali A0L3M0.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 156889.Mmc1_0034.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABK42563 ; ABK42563 ; Mmc1_0034 .
GeneIDi 4480720.
KEGGi mgm:Mmc1_0034.
PATRICi 22426524. VBIMagSp23654_0034.

Phylogenomic databases

eggNOGi COG0502.
HOGENOMi HOG000239958.
KOi K01012.
OMAi TCENTLR.
OrthoDBi EOG622PMP.

Enzyme and pathway databases

UniPathwayi UPA00078 ; UER00162 .
BioCyci MSP156889:GH36-34-MONOMER.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_01694. BioB.
InterProi IPR013785. Aldolase_TIM.
IPR010722. BATS_dom.
IPR002684. Biotin_synth/BioAB.
IPR024177. Biotin_synthase.
IPR006638. Elp3/MiaB/NifB.
IPR007197. rSAM.
[Graphical view ]
Pfami PF06968. BATS. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view ]
PIRSFi PIRSF001619. Biotin_synth. 1 hit.
SMARTi SM00876. BATS. 1 hit.
SM00729. Elp3. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00433. bioB. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MC-1.

Entry informationi

Entry nameiBIOB_MAGSM
AccessioniPrimary (citable) accession number: A0L3M0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: December 12, 2006
Last modified: November 26, 2014
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3